期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1973
卷号：70
期号：7
页码：1943-1946
DOI：10.1073/pnas.70.7.1943
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：A well-characterized line of rat Schwann cells has been examined for its ability to produce collagen. About 14% of the [3H]proline in the proteins that were secreted into the culture medium by the cells was hydroxylated, while only 1% of the labeled proteins in the cell layer contained [3H]hydroxyproline. Three sizes of procollagen polypeptides, of molecular weights about 105,000, 120,000, and 155,000, were present in the medium, as well as tropocollagen molecules that contained the usual [α]1 and [α]2 chains. Subsequently, the Schwann cells ceased producing the smaller collagenous polypeptides, although the total [3H]hydroxyproline content of the medium was unchanged. The [3H]hydroxyproline was almost entirely accounted for by the polypeptide of 155,000 daltons; this peptide was rapidly digested by collagenase or pepsin or chymotrypsin. The destruction by pepsin and chymotrypsin indicates that the large polypeptide, in contrast to procollagen and tropocollagen, is not in the collagenous (helical) conformation. Possibly, this substance is a very early form of procollagen that does not fold into the collagen conformation. The data show that cells of neuroectodermal origin can synthesize collagen, and also suggest that Schwann cells may be responsible for a large proportion of the collagen seen in peripheral neurinomas in vivo.
关键词：peripheral neurinoma ; acrylamide gel electrophoresis ; S100 protein ; myelin basic protein
